305-84-0Relevant articles and documents
Molecular identification of carnosine synthase as ATP-grasp domain-containing protein 1 (ATPGD1)
Drozak, Jakub,Veiga-da-Cunha, Maria,Vertommen, Didier,Stroobant, Vincent,Van Schaftingen, Emile
, p. 9346 - 9356 (2010)
Carnosine (β-alanyl-L-histidine) and homocarnosine (γ-aminobutyryl-L-histidine) are abundant dipeptides in skeletal muscle and brain of most vertebrates and some invertebrates. The formation of both compounds is catalyzed by carnosine synthase, which is thought to convert ATP to AMP and inorganic pyrophosphate, and whose molecular identity is unknown. In the present work, we have purified carnosine synthase from chicken pectoral muscle about 1500-fold until only two major polypeptides of 100 and 90 kDa were present in the preparation. Mass spectrometry analysis of these polypeptides did not yield any meaningful candidate. Carnosine formation catalyzed by the purified enzyme was accompanied by a stoichiometric formation, not of AMP, but of ADP, suggesting that carnosine synthase belongs to the "ATP-grasp family" of ligases. A data base mining approach identified ATPGD1 as a likely candidate. As this protein was absent from chicken protein data bases, we reconstituted its sequence from a PCR-amplified cDNA and found it to fit with the 100-kDa polypeptide of the chicken carnosine synthase preparation. Mouse and human ATPGD1 were expressed in HEK293T cells, purified to homogeneity, and shown to catalyze the formation of carnosine, as confirmed by mass spectrometry, and of homocarnosine. Specificity studies carried out on all three enzymes were in agreement with published data. In particular, they acted with 15-25-fold higher catalytic efficiencies on β-alanine than on γ-aminobutyrate. The identification of the gene encoding carnosine synthase will help for a better understanding of the biological functions of carnosine and related dipeptides, which still remain largely unknown.
Solid-phase peptide synthesis of dipeptide (histidine-β-Alanine) as a chelating agent by using trityl chloride resin, for removal of Al3+, Cu2+, Hg2+ and Pb2+: Experimental and theoretical study
Rahimi, Rahmatollah,Khosravi, Maryam,Tehrani, Mohammd H. H.,Rabbani, Mahboubeh,Safavi, Ebrahim
, p. 1814 - 1819 (2016)
Solid-phase peptide synthesis of dipeptide (histidine-β-Alanine) as a chelating agent examined by common N-9-fluorenylmethyloxycarbonyl-N-Trityl-L-histidine and tert-butyloxycarbonyl-β-Alanine-OH amino acid derivatives. Trityl chloride resin was used as a carrier resin. The molecular structure of the dipeptide was definite by using different methods such as ultraviolet visible (UV-Vis), Fourier transform infrared (FTIR), proton (1H) nuclear magnetic ressonance (NMR) and liquid chromatography-mass spectrometry (LC-MS) and the chelating property of synthesized dipeptide was investigated for removing of metal ions Al3+, Cu2+, Hg2+ and Pb2+ in vitro. In addition, the pharmacological and biological activities of dipeptide were examined by prediction of activity spectra for substances (PASS) program.
Carnosine intermediate and preparation and application of carnosine thereof
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Paragraph 0039; 0040, (2022/03/27)
The invention provides a carnosine intermediate and preparation and application of carnosine thereof, and belongs to the technical field of medical intermediates. The preparation method of the carnosine intermediate comprises the following steps: carrying out acylation reaction on L-histidine and tert-butyl cyanoacetate under the action of a catalyst to prepare the carnosine intermediate; wherein isonicotinic acid and 4-chloropyrimidine are added as catalytic assistants. When the carnosine intermediate is prepared, isonicotinic acid and 4-chloropyrimidine are used as auxiliaries, and the yield of the obtained carnosine intermediate is greatly improved. The method for preparing carnosine from the carnosine intermediate prepared by the method comprises the step of adding a catalyst into the carnosine intermediate for catalytic hydrogenation reduction to obtain the carnosine. The composition prepared from the obtained carnosine, theanine and loganic acid has the effects of resisting oxidation and whitening.
METHODS AND COMPOSITIONS FOR RAPIDLY DECREASING EPIGENETIC AGE AND RESTORATION OF MORE YOUTHFUL FUNCTION
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, (2020/03/01)
Disclosed are methods and compositions of reducing the epigenetic age of mammalian organism, especially an adult human of geriatric age. The methods provide for the proliferation of endogenous stem cells using mitochondrial fusion and a UCP2 blocker or other stimulants; supplying stem cells with nutrition to prevent cell cycle arrest; and removal of senescent somatic cells using senolytic treatments. The proliferation of endogenous neural stem cells after plaque removal for the treatment of Alzheimer's is also disclosed.
A green-by-design bioprocess for l-carnosine production integrating enzymatic synthesis with membrane separation
Yin, Dong-Ya,Pan, Jiang,Zhu, Jie,Liu, You-Yan,Xu, Jian-He
, p. 5971 - 5978 (2019/11/14)
l-Carnosine (l-Car, β-alanyl-l-histidine) is a bioactive dipeptide with important physiological functions. Direct coupling of unprotected β-Ala (β-alanine) with l-His (l-histidine) mediated by an enzyme is a promising method for l-Car synthesis. In this study, a new recombinant dipeptidase (SmPepD) from Serratia marcescens with a high synthetic activity toward l-Car was identified by a genome mining approach and successfully expressed in Escherichia coli. Divalent metal ions strongly promoted the synthetic activity of SmPepD, with up to 21.7-fold increase of activity in the presence of 0.1 mM MnCl2. Higher temperature, lower pH and increasing substrate loadings facilitated the l-Car synthesis. Pilot biocatalytic syntheses of l-Car were performed comparatively in batch and continuous modes. In the continuous process, an ultra-filtration membrane reactor with a working volume of 5 L was employed for catalyst retention. The dipeptidase, SmPepD, showed excellent operational stability without a significant decrease in space-time yield after 4 days. The specific yield of l-Car achieved was 105 gCar gcatalyst-1 by the continuous process and 30.1 gCar gcatalyst-1 by the batch process. A nanofiltration membrane was used to isolate the desired product l-Car from the reaction mixture by selectively removing the excess substrates, β-Ala and l-His. As a result, the final l-Car content was effectively enriched from 2.3% to above 95%, which gave l-Car in 99% purity after ethanol precipitation with a total yield of 60.2%. The recovered substrate mixture of β-Ala and l-His can be easily reused, which will enable the economically attractive and environmentally benign production of the dipeptide l-Car.
METHOD FOR PREPARING PEPTIDES
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Page/Page column 73, (2019/06/11)
The invention relates to a method for preparing peptides comprising the step of forming a peptide bond wherein at least one amino acid or peptide comprises a protecting group having a water-solubility enhancing group, and said forming of a peptide bond is achieved while an amino acid or a peptide is bound to a solid phase. The invention further relates to peptides comprising a protecting group having a water-solubility enhancing group being bound to the amino group and an activated or free carboxyl group.
METHOD FOR PRODUCING L-CARNOSINE DERIVATIVE AND L-CARNOSINE
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, (2019/12/05)
PROBLEM TO BE SOLVED: To provide a convenient method for producing a high-purity N-protected L-carnosine derivative and L-carnosine. SOLUTION: A production method includes reacting an acid halide (1) with an L-histidine derivative (2). (R1 and R2 are H or a protection group of an amino group; X is a halogen atom). (A TMS group is a trimethylsilyl group). SELECTED DRAWING: None COPYRIGHT: (C)2020,JPOandINPIT
METHOD FOR PREPARING PEPTIDES
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Page/Page column 66-67, (2019/06/11)
The invention relates to a method for preparing peptides comprising the step of forming a peptide bond wherein the carboxyl group of a first amino acid or first peptide is activated and an amino group of the first activated amino acid or first peptide is protected by a protecting group having a water-solubility enhancing group and the activated carboxyl group of the first amino acid or first peptide is reacted with an amino group of a second amino acid or second peptide wherein said carboxyl group of the first amino acid or first peptide is activated in the absence of the second amino acid or second peptide. The invention further relates to peptides comprising a protecting group having a water-solubility enhancing group being bound to the amino group and an activated or free carboxyl group.
Synthetic method of L-carnosine
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Paragraph 0005; 0032; 0033; 0034; 0035, (2017/08/28)
The invention discloses a synthetic method of L-carnosine, and belongs to the technical field of organic matter synthesis. The method comprises the following steps: dissolving 3-chloropropionic acid in an organic solvent, and converting the 3-chloropropionic acid by a chloroformylation reagent to form corresponding 3-chloropropionyl chloride; condensing trimethylsilane protected L-histidine and the 3-chloropropionyl chloride to obtain a corresponding amide product; removing protection agents by using water or an alkaline solution to obtain an intermediate; carrying out aminolysis on the intermediate to obtain crude L-carnosine; and purifying the crude L-carnosine to obtain finished L-carnosine. The synthetic method has the advantages of low raw material consumption, short reaction steps, few wastes, high yield, obtaining of high-quality L-carnosine free from hydrazine, and meeting of industrial production demands.
Concise Synthesis of Anserine: Efficient Solvent Tuning in Asymmetric Hydrogenation Reaction
Yamashita, Megumi,Shimizu, Keita,Koizumi, Yasuaki,Wakimoto, Toshiyuki,Hamashima, Yoshitaka,Asakawa, Tomohiro,Inai, Makoto,Kan, Toshiyuki
supporting information, p. 2734 - 2736 (2016/11/30)
A concise synthesis of anserine and related compounds was accomplished by Et-DuPhos-Rh-catalyzed asymmetric hydrogenation of dehydrohistidine derivatives in 2,2,2-trifluoroethanol, which played a key role in improving the yield and selectivity.
